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Human LIF Recombinant (CHO cell)

LIF

accession:  P15018
   Size A     10ug   $ 160
   Size B      50ug  $480
   Size C      1mg  $ 3500
Domain  :  4 helix cytokine core
Gene  :  LIF
Catalog no. :  RCP15018
Source:
Optimized DNA sequence encoding Human LIF mature chain was expressed in CHO Cells

 
Molecular weight:

Native human LIF is generated by the proteolytic removal of the signal peptide
and propeptide,  the molecule has a calculated molecular mass of approximately 20 kDa.

LIF is a disulfide-linked monomer protein consisting of 181 amino acid residue subunits, and migrates as an approximately 36 kDa protein under  reducing conditions in SDS-PAGE.


 
Purity:
>95%, as determined by SDS-PAGE and HPLC.

 
Biological Activity:
The ED(50) was determined by the proliferation of Human TF-1 cells and  was found to be  < 0.1 ng/ml.

 
Protein Sequence:
        10         20         30         40         50         60 
MKVLAAGVVP LLLVLHWKHG AGSPLPITPV NATCAIRHPC HNNLMNQIRS QLAQLNGSAN 

        70         80         90        100        110        120 
ALFILYYTAQ GEPFPNNLDK LCGPNVTDFP PFHANGTEKA KLVELYRIVV YLGTSLGNIT 

       130        140        150        160        170        180 
RDQKILNPSA LSLHSKLNAT ADILRGLLSN VLCRLCSKYH VGHVDVTYGP DTSGKDVFQK 

       190        200 
KKLGCQLLGK YKQIIAVLAQ AF 
(*)Complete precursor sequence shown, expressed chain highlighted
 
Endotoxin:
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).

 
Presentation:
Recombinant  Leukemia Inhibitory Factor was lyophilized from a 0.2 μm filtered PBS pH 4.5.

 
Reconstitution:
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers

 
Storage:
The lyophilized protein is stable for at least 2 years from date of receipt at -20° C.
Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8° C for one month, or at -20° C for six months, with a carrier protein without detectable loss of activity.

Avoid repeated freeze/thaw cycles.

 
Usage:
This cytokine product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.

 

Leukemia Inhibitory Factor

LIF, a multifunctional, secreted glycoprotein that exists in both soluble and matrix-bound forms, displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation. It is now clear that LIF is related in both structure and mechanism of action to the interleukin (IL)-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1. The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130.

Related Publications:
socs1, socs3, and pias1 promote myogenic differentiation by inhibiting the Leukemia Inhibitory Factor-induced jak1/stat1/stat3 pathway
Mol. Cell. Biol., Sep 2009; 29: 5084 - 5093.
interleukin-11 and Leukemia Inhibitory Factor regulate the adhesion of endometrial epithelial cells: implications in fertility regulation
Endocrinology, Jun 2009; 150: 2915 - 2923.
Leukemia Inhibitory Factor controls a retinal rescue mechanism which supports survival of photoreceptor cells in vivo
Invest. Ophthalmol. Vis. Sci., Apr 2009; 50: 3880.
Leukemia Inhibitory Factor (lif) induces protection of photoreceptors from light damage without reducing oxidative injury
Invest. Ophthalmol. Vis. Sci., Apr 2009; 50: 682.
prokineticin 1 mediates fetal-maternal dialogue regulating endometrial Leukemia Inhibitory Factor
FASEB J, Jul 2009; 23: 2165 - 2175.




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